RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae

被引:115
作者
Ivanyi-Nagy, Roland [1 ]
Lavergne, Jean-Pierre [2 ]
Gabus, Caroline [1 ]
Ficheux, Damien [2 ]
Darlix, Jean-Luc [1 ]
机构
[1] Ecole Normale Super Lyon, IFR Biosci Lyon Gerland 128, INSERM, U758, F-69364 Lyon 07, France
[2] Univ Lyon 1, IFR Biosci Lyon Gerland 128, UMR CNRS 5086, Inst Biol & Chim Proteines, F-69367 Lyon 07, France
关键词
D O I
10.1093/nar/gkm1051
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
RNA chaperone proteins are essential partners of RNA in living organisms and viruses. They are thought to assist in the correct folding and structural rearrangements of RNA molecules by resolving misfolded RNA species in an ATP-independent manner. RNA chaperoning is probably an entropy-driven process, mediated by the coupled binding and folding of intrinsically disordered protein regions and the kinetically trapped RNA. Previously, we have shown that the core protein of hepatitis C virus (HCV) is a potent RNA chaperone that can drive profound structural modifications of HCV RNA in vitro. We now examined the RNA chaperone activity and the disordered nature of core proteins from different Flaviviridae genera, namely that of HCV, GBV-B (GB virus B), WNV (West Nile virus) and BVDV (bovine viral diarrhoea virus). Despite low-sequence similarities, all four proteins demonstrated general nucleic acid annealing and RNA chaperone activities. Furthermore, heat resistance of core proteins, as well as far-UV circular dichroism spectroscopy suggested that a well-defined 3D protein structure is not necessary for core-induced RNA structural rearrangements. These data provide evidence that RNA chaperoningpossibly mediated by intrinsically disordered protein segmentsis conserved in Flaviviridae core proteins. Thus, besides nucleocapsid formation, core proteins may function in RNA structural rearrangements taking place during virus replication.
引用
收藏
页码:712 / 725
页数:14
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